Cytochrome c structure
P99999
CYC_HUMAN
CYCS

Cytochrome c

Homo sapiensTaxon: 9606

3D-structureAcetylationApoptosisDirect protein sequencingDisease variantElectron transportHemeIronMetal-bindingMitochondrionPhosphoproteinProteomics identification+3
Sequence Length

105

amino acids

Molecular Weight

11.7 kDa

theoretical

Experimental Structures

13

PDB entries

Related Diseases

1

recorded

Function

Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases

Related Diseases

Thrombocytopenia 4

A form of thrombocytopenia, a hematologic disorder defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting.

Amino Acid Sequence

MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIW
GEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE

FASTA format · 105 amino acids · mass 11.7 kDa

Experimental Structures

13 PDB entries
1J3S2N3Y2N9I2N9J3NWV3ZCF3ZOO5EXQ5O105TY36DUJ6ECJ6XNK

Post-Translational Modifications

  • Binds 1 heme c group covalently per subunit
  • Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the turnover in the reaction with cytochrome c oxidase, down-regulating mitochondrial respiration